Open AccessIdentification of a Novel Consensus Sequence at the Cleavage Site of the Lassa Virus Glycoprotein
Author(s) -
Oliver Lenz,
Jan ter Meulen,
Heinz Feldmann,
HansDieter Klenk,
Wolfgang Garten
Publication year - 2000
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.74.23.11418-11421.2000
Subject(s) - biology , edman degradation , lassa virus , glycoprotein , cleavage (geology) , peptide sequence , virology , microbiology and biotechnology , proteolysis , sequence motif , virus , biochemistry , enzyme , paleontology , fracture (geology) , gene , dna
The Lassa virus glycoprotein consists of an amino-terminal and a carboxy-terminal cleavage fragment designated GP-1 and GP-2, respectively, that are derived by proteolysis from the precursor GP-C. The membrane-anchored GP-2 obtained from purified virions of the Josiah strain revealed the N-terminal tripeptide GTF262 when analyzed by Edman degradation. Upstream of this site, GP-C contains the tetrapeptide sequence RRLL259 , which is conserved in all Lassa virus isolates published to date. Systematic mutational analysis of vector-expressed GP-C revealed that the motif R-X (L/I/V)-L259 (where X stands for L, I, or V) is essential for cleavage of the peptide bond between leucine259 and glycine260 . This cleavage motif is homologous to the consensus sequence recognized by a novel class of cellular endoproteases which have so far not been implicated in the processing of viral glycoproteins.